3EQT

Crystal structure of human LGP2 C-terminal domain in complex with dsRNA

Summary for 3EQT

• Entry DOI: 10.2210/pdb3eqt/pdb
• Descriptor: ATP-dependent RNA helicase DHX58, 5'-R(*GP*CP*GP*CP*GP*CP*GP*C)-3', ZINC ION, ... (4 entities in total)
• Functional Keywords: innate immunity, rig-i-like helicases, viral rna detection, lgp2-dsrna complex, atp-binding, coiled coil, cytoplasm, helicase, hydrolase, immune response, nucleotide-binding, polymorphism, rna-binding, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm: Q96C10
• Total number of polymer chains: 4
• Total formula weight: 38682.36

Authors

Li, P.,Li, X. (deposition date: 2008-10-01, release date: 2009-03-10, Last modification date: 2023-09-06)

Primary citation

Li, X.,Ranjith-Kumar, C.T.,Brooks, M.T.,Dharmaiah, S.,Herr, A.B.,Kao, C.,Li, P.
The RIG-I-like Receptor LGP2 Recognizes the Termini of Double-stranded RNA
J.Biol.Chem., 284:13881-13891, 2009

PubMed Abstract: The RIG-I-like receptors (RLRs), RIG-I and MDA5, recognize single-stranded RNA with 5' triphosphates and double-stranded RNA (dsRNA) to initiate innate antiviral immune responses. LGP2, a homolog of RIG-I and MDA5 that lacks signaling capability, regulates the signaling of the RLRs. To establish the structural basis of dsRNA recognition by the RLRs, we have determined the 2.0-A resolution crystal structure of human LGP2 C-terminal domain bound to an 8-bp dsRNA. Two LGP2 C-terminal domain molecules bind to the termini of dsRNA with minimal contacts between the protein molecules. Gel filtration chromatography and analytical ultracentrifugation demonstrated that LGP2 binds blunt-ended dsRNA of different lengths, forming complexes with 2:1 stoichiometry. dsRNA with protruding termini bind LGP2 and RIG-I weakly and do not stimulate the activation of RIG-I efficiently in cells. Surprisingly, full-length LGP2 containing mutations that abolish dsRNA binding retained the ability to inhibit RIG-I signaling.

PubMed: 19278996
DOI: 10.1074/jbc.M900818200

Experimental method

X-RAY DIFFRACTION (2 Å)